ArticleMolecular biology of the cell2022
Docking of Syk to FcεRI is enhanced by Lyn but limited in duration by SHIP1.
Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- IgE Occupancy and Antigen Valency Cooperate to Control FcεRI Aggregation Geometry and Signaling Efficiency.International journal of molecular sciences · 2026Article
- Neuroimmune Regulation of Microvascular Inflammation: The Heart-Brain Axis, Mast Cells, and the Protective Role of Flavonoids-A Comprehensive Review.Biomedicines · 2026Review
- The SHIP1-inflammatory-lipid axis in Alzheimer's disease: from genetic risk to spatiotemporal mechanistic insights.Journal of neuroinflammation · 2026Review
- IgE occupancy and antigen valency cooperate to control FcεRI aggregation geometry and signaling efficiency.bioRxiv : the preprint server for biology · 2025Article
- Antigen properties shape organization of FcεRI aggregates to tune mast cell signaling.bioRxiv : the preprint server for biology · 2025Article
- Bayesian Inference of Binding Kinetics from Fluorescence Time Series.The journal of physical chemistry. B · 2025Article
- The role of immunoglobulin E in non-atopic disorders.Frontiers in immunology · 2025Review
- The role of mast cells in allergic rhinitis.PeerJ · 2025Review
- Allergenic protein-induced type I hypersensitivity models: a review.Frontiers in allergy · 2024Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The high-affinity immunoglobulin E (IgE) receptor, FcεRI, is the primary immune receptor found on mast cells and basophils. Signal initiation is classically attributed to phosphorylation of FcεRI β- and γ-subunits by the Src family kinase (SFK) Lyn, followed by the recruitment and activation of the tyrosine kinase Syk. FcεRI signaling is tuned by the balance between Syk-driven positive signaling and the engagement of inhibitory molecules, including SHIP1. Here, we investigate the mechanistic contributions of Lyn, Syk, and SHIP1 to the formation of the FcεRI signalosome. Using Lyn-deficient RBL-2H3 mast cells, we found that another SFK can weakly monophosphorylate the γ-subunit, yet Syk still binds the incompletely phosphorylated immunoreceptor tyrosine-based activation motifs (ITAMs). Once recruited, Syk further enhances γ-phosphorylation to propagate signaling. In contrast, the loss of SHIP1 recruitment indicates that Lyn is required for phosphorylation of the β-subunit. We demonstrate two noncanonical Syk binding modes,
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.